The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Essential Biochemistry and Physiology of (NT-pro)BNP
Abstract
Brain natriuretic peptide (BNP) is a 32 amino acid cardiac natriuretic peptide hormone originally isolated from porcine brain tissue. The human BNP gene is located on chromosome 1 and encodes the prohormone proBNP. The biologically active BNP and the remaining part of the prohormone, NT-proBNP (76 amino acids) can be measured by immunoassay in human blood. Cardiac myocytes constitute the major source of BNP related peptides. The main stimulus for peptide synthesis and secretion is myocyte stretch. Recently, cardiac fibroblasts have also been shown to produce BNP. Other neurohormones may stimulate cardiac BNP production in different cardiac cell types. In contrast to atrial natriuretic peptides (ANP/NT-proANP), which originate mainly from atrial tissue, BNP related peptides are produced mainly from ventricular myocytes. Ventricular (NT-pro)BNP production is strongly upregulated in cardiac failure and locally in the area surrounding a myocardial infarction. In peripheral organs BNP binds to the natriuretic peptide receptor type A causing increased intracellular cGMP production. The biological effects include diuresis, vasodilatation, inhibition of renin and aldosterone production and of cardiac and vascular myocyte growth. In mice BNP gene knockout leads to cardiac fibrosis, gene over-expression to hypotension and bone malformations. BNP is cleared from plasma through binding to the natriuretic peptide clearance receptor type C, but it seems relatively resistant to proteolysis by neutral endopeptidase NEP 24.11. Clearance mechanisms for NT-proBNP await further study. While the plasma concentration of NT-proBNP and BNP is approximately equal in normal controls, NT-proBNP plasma concentration is 2–10 times higher than BNP in patients with heart failure. This relative change in peptide levels may be explained by shifts in cardiac secretion and/or clearance mechanisms.
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Kragelund, C., Grønning, B., Køber, L., Hildebrandt, P., & Steffensen, R. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa042330 · Cited by 631
Plasma Adiponectin, Body Mass Index, and Mortality in Patients With Chronic Heart Failure
Kistorp, C., Faber, J., Galatius, S., Gustafsson, F., Frystyk, J., Flyvbjerg, A., & Hildebrandt, P. (2005) · Circulation · doi:10.1161/circulationaha.104.530972 · Cited by 605
The future of drug safety testing: expanding the view and narrowing the focus
Stevens, J. L., & Baker, T. K. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2008.11.009 · Cited by 286
N-Terminal Pro-Brain Natriuretic Peptide Levels and Risk of Death in Sickle Cell Disease
Machado, R. F., Anthi, A., Steinberg, M. H., Bonds, D., Sachdev, V., Kato, G. J., Taveira-DaSilva, A. M., Ballas, S. K., Blackwelder, W., Xu, X., et al. (2006) · JAMA · doi:10.1001/jama.296.3.310 · Cited by 197
Metadata
- Authors
- Hall, C.
- Venue
- European Journal of Heart Failure
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-03-01
- Volume
- 6
- Issue
- 3
- Pages
- 257-260
- ISSN
- 1388-9842 (ISSN-L)
- 1879-0844
- OpenAlex
- W2014112740
- Cited by
- 565
- References
- 16
- FWCI
- 19.41
- Type
- journal article
- Language
- en
- Open access
- closed
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